{"id":49646,"date":"2020-10-19T00:00:00","date_gmt":"2020-10-18T23:00:00","guid":{"rendered":"http:\/\/www.pcb.ub.edu\/researchers-discover-the-adhesion-mechanism-of-the-bacterium-that-causes-40-of-atypical-pneumonias\/"},"modified":"2020-11-18T14:56:07","modified_gmt":"2020-11-18T13:56:07","slug":"researchers-discover-the-adhesion-mechanism-of-the-bacterium-that-causes-40-of-atypical-pneumonias","status":"publish","type":"post","link":"https:\/\/www.pcb.ub.edu\/en\/researchers-discover-the-adhesion-mechanism-of-the-bacterium-that-causes-40-of-atypical-pneumonias\/","title":{"rendered":"Researchers discover the adhesion mechanism of the bacterium that causes 40% of atypical pneumonias"},"content":{"rendered":"

Mycoplasma pneumoniae<\/em> is a human pathogen that causes up to 40% of atypical primary pneumonias, a type of\u00a0respiratory infections\u00a0that can lead to serious complications.\u00a0In fact, it is estimated that in 25% of cases, symptoms can\u00a0spread out of the lungs\u00a0and cause neurological, hepatic or cardiac effects.<\/p>\n

Now, a\u00a0team of researchers led by David Aparicio, from\u00a0Institute of Molecular Biology of Barcelona (IBMB-CSIC),\u00a0and Makoto Miyata, from the Institute for Natural Science and Technology at the University of Osaka,\u00a0have discovered the mechanism by which the bacteria that cause 40% of atypical pneumonias adhere to the lungs, which has allowed them to design antibodies that decrease this adhesion capacity and opens the door to\u00a0develop new therapies\u00a0and vaccines against this pathogen.<\/p>\n

The work, whose first author is David Vizarraga, predoctoral researcher at the IBMB-CSIC, will allow\u00a0develop new therapeutic strategies\u00a0based on adhesion blocking, a mechanism that was already known, but the structure of the proteins involved in this process had never been determined.<\/p>\n

A mechanism based on an adhesion complex<\/strong><\/span><\/p>\n

Mycoplasma pneumoniae is a human pathogen that causes up to 40% of atypical primary pneumonias, a type of\u00a0respiratory infections\u00a0that can lead to serious complications.\u00a0In fact, it is estimated that in 25% of cases, symptoms can\u00a0spread out of the lungs\u00a0and cause neurological, hepatic or cardiac effects.<\/p>\n

It was known, for example, that the bacterium adheres to cell receptors that are generically known\u00a0by the name of sialic acids, receptors that are used by other important pathogens to bind to cells, such as the bacterium Mycoplasma genitalium or the influenza virus.<\/p>\n

At the Institute of Molecular Biology of Barcelona of the CSIC they have obtained crystals that contained the proteins P1 and P40 \/ P90 bound to sialic acids and have analyzed them with X-rays, in the Xaloc line of the ALBA Syncroton, which has allowed\u00a0visualize the three-dimensional structure\u00a0of these proteins.<\/p>\n

\u201cWe have seen that the binding site for sialic acids is in P40 \/ P90 and not in the P1 protein, as previously thought, and we have identified two well-differentiated parts in the P1 protein, one with a\u00a0high genetic variability\u00a0and clinical (in the N-terminal region) and another much more conserved (in the C-terminal end) \u201c, has detailed Aparicio.<\/p>\n

\u201cThis information has helped us\u00a0design antibodies\u00a0that bind to the most conserved part of the protein in order to block the adhesion of the bacteria to human cells \u201c, added Vizarraga.<\/p>\n

According to the researcher at the Hospital Parc Taul\u00ed, \u00d3scar Quijada, \u201ctrials with patients infected by Mycoplasma pneumoniae reveal that the C-terminal end of the P1 protein generates a\u00a0strong immune response\u00a0and in the long term, characteristics that make it an ideal candidate for vaccine development.”<\/p>\n

\u25ba Reference article:<\/strong> Immunodominant proteins P1 and P40\/P90 from human pathogen Mycoplasma pneumoniae<\/em>. Vizarraga et al.Nature Communications, https:\/\/doi.org\/10.1038\/s41467-020-18777-y<\/a><\/p>\n

\u25ba\u00a0More information:\u00a0IBMB-CSIC website [+]<\/a><\/strong><\/p>\n","protected":false},"excerpt":{"rendered":"

Researchers from Institute of Molecular Biology of Barcelona (IBMB-CSIC<\/a>) \u2013based in the Barcelona Science Park\u2013 and\u00a0the Institute for Natural Science and Technology <\/a>at the University of Osaka, has succeeded in determining the three-dimensional structure of proteins by means of which the bacteria Mycoplasma pneumoniae<\/em> \u2013that cause 40% of atypical pneumonias\u2013 attaches itself to human cells and initiates infection. From the structure, this team of scientists have designed antibodies that decrease this adhesion capacity and opens the door to develop new therapies and vaccines against this pathogen.<\/p>\n

\u00a0<\/p>\n","protected":false},"author":1,"featured_media":53698,"comment_status":"closed","ping_status":"open","sticky":false,"template":"","format":"standard","meta":{"_acf_changed":false,"inline_featured_image":false,"footnotes":""},"categories":[36],"tags":[],"class_list":["post-49646","post","type-post","status-publish","format-standard","has-post-thumbnail","category-science"],"acf":[],"yoast_head":"\nResearchers discover the adhesion mechanism of the bacterium that causes 40% of atypical pneumonias - Parc Cient\u00edfic de Barcelona<\/title>\n<meta name=\"robots\" content=\"index, follow, max-snippet:-1, max-image-preview:large, max-video-preview:-1\" \/>\n<link rel=\"canonical\" href=\"https:\/\/www.pcb.ub.edu\/en\/researchers-discover-the-adhesion-mechanism-of-the-bacterium-that-causes-40-of-atypical-pneumonias\/\" \/>\n<meta property=\"og:locale\" content=\"en_US\" \/>\n<meta property=\"og:type\" content=\"article\" \/>\n<meta property=\"og:title\" content=\"Researchers discover the adhesion mechanism of the bacterium that causes 40% of atypical pneumonias - Parc Cient\u00edfic de Barcelona\" \/>\n<meta property=\"og:description\" content=\"Researchers from Institute of Molecular Biology of Barcelona (IBMB-CSIC) \u2013based in the Barcelona Science Park\u2013 and\u00a0the Institute for Natural Science and Technology at the University of Osaka, has succeeded in determining the three-dimensional structure of proteins by means of which the bacteria Mycoplasma pneumoniae \u2013that cause 40% of atypical pneumonias\u2013 attaches itself to human cells and initiates infection. 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